Article
The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.
The Journal of biological chemistry - 11 Jun 2010
Langelier Marie-France, Ruhl Donald D, Planck Jamie L, Kraus W Lee, Pascal John M
Abstract excerpt
PARP-1 is involved in multiple cellular processes, including transcription, DNA repair, and apoptosis. PARP-1 attaches ADP-ribose units to target proteins, including itself as a post-translational modification that can change the biochemical properties of target proteins and mediate recruitment of proteins to sites of poly(ADP-ribose) synthesis. Independent of its catalytic activity, PARP-1 binds to chromatin and...
Topics
- Adenosine Diphosphate
- Chromatin
- Cloning, Molecular
- Dimerization
- Humans
- Kinetics
- Mutagenesis, Site-Directed
- Mutation
- Poly (ADP-Ribose) Polymerase-1
- Poly(ADP-ribose) Polymerases
- Protein Structure, Tertiary
- RNA Polymerase II
- Transcription, Genetic
